Component

Human cytochrome c oxidase assembly protein SCO1

Human cytochrome c oxidase assembly protein SCO1. Species, exposure and limitations are retained in each linked claim.

4 recorded relationships. Experimental role, claim status and evidence remain attached to each record.

Read recorded mechanisms Open recursive mind map

How nutrients influence it

Every nutrient with a recorded effect on this component, credited to the nutrient that acted rather than the chapter that recorded it. Open a nutrient to see the findings and the conditions they were measured under.

How nutrients reach it in more than one step

Chains of two or more recorded steps that end here, grouped by the nutrient they start from. Each step is a separate finding, so a chain is a route a mechanism could take, not proof that it does.

Tracing routes…

What it does

Every recorded relationship this component is part of, grouped by its role. Plain wording comes first; the technical statement follows.

Recorded relationships

What it acts on

  1. SCO1-associated cellular copper deficiency reflected increased copper efflux rather than reduced high-affinity uptake in the studied patient-cell models.

    Human cytochrome c oxidase assembly protein SCO1 → Cellular copper efflux source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_span
    {"source_cache": "artifacts/copper-research/17189203.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "7653227df0fe557c484a72eafed6a7a96dc06f5d4f63f7eea4a5b9568949a698", "start_char": 0, "end_char": 950, "text_sha256": "7653227df0fe557c484a72eafed6a7a96dc06f5d4f63f7eea4a5b9568949a698"}
    experimental_model
    SCO1/SCO2 patient-cell analysis and genetic complementation
    exposure
    Pathogenic SCO variants; transporter and rescue assays
    limitations
    Copper effects varied with allele and tissue. A genetic assembly defect does not prove inadequate intake or universal response to copper supplementation.
    nutrient_topic
    Copper research collection; topical membership is not evidence of a direct dietary effect. · Copper
    organism
    Human
    plain_language
    The problem was copper leaving the cell too quickly.
    primary_references
    [copper-p17189203] The human cytochrome c oxidase assembly factors SCO1 and SCO2 have regulatory roles in the maintenance of cellular copper homeostasis. (2007). https://pubmed.ncbi.nlm.nih.gov/17189203/ DOI: 10.1016/j.cmet.2006.12.001
    tissue_or_cell_type
    Patient-derived cellular systems
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Copper: transport, cuproenzymes, deficiency, excess and nutrient interactions (2026-09-17) · lines 702–713

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · SCO1/SCO2 patient-cell analysis and genetic complementation · source_derived_draft · unverified_draft

    ### copper-sco1-copper-efflux SCO1-associated cellular copper deficiency reflected increased copper efflux rather than reduced high-affinity uptake in the studied patient-cell models. Condition category: machinery_impairment nutrient_topic: Copper research collection; topical membership is not evidence of a direct dietary effect. plain_language: The problem was copper leaving the cell too quickly. organism: Human tissue_or_cell_type: Patient-derived cellular systems experimental_model: SCO1/SCO2 patient-cell analysis and genetic complementation limitations: Copper effects varied with allele and tissue. A genetic assembly defect does not prove inadequate intake or universal response to copper supplementation. exposure: Pathogenic SCO variants; transporter and rescue assays evidence_span: {"source_cache": "artifacts/copper-research/17189203.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "7653227df0fe557c484a72eafed6a7a96dc06f5d4f63f7eea4a5b9568949a698", "start_char": 0, "end_char": 950, "text_sha256": "7653227df0fe557c484a72eafed6a7a96dc06f5d4f63f7eea4a5b9568949a698"} [copper-p17189203] The human cytochrome c oxidase assembly factors SCO1 and SCO2 have regulatory roles in the maintenance of cellular copper homeostasis. (2007). https://pubmed.ncbi.nlm.nih.gov/17189203/ DOI: 10.1016/j.cmet.2006.12.001
    Complete structured claim and evidence

What acts on it

  1. COA6 acted as a thiol reductase for critical cysteine disulfides in SCO1.

    Human cytochrome c oxidase assembly factor COA6 → Human cytochrome c oxidase assembly protein SCO1 source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/copper-research/32061935.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "7a7828c0b3a9e17878ed230d32af9dd51b667cd1ef0c934fb299f15b5a5e2b0a", "start_char": 0, "end_char": 1043, "text_sha256": "7a7828c0b3a9e17878ed230d32af9dd51b667cd1ef0c934fb299f15b5a5e2b0a"}
    experimental_model
    COA6 knockout HEK293T cells and biochemical protein interaction experiments
    exposure
    COA6 loss; SCO1/SCO2 disulfide reduction assays
    limitations
    COA6 machinery failure is not dietary copper depletion. Protein import effects were selective rather than universal loss of all mitochondrial import.
    nutrient_topic
    Copper research collection; topical membership is not evidence of a direct dietary effect. · Copper
    organism
    Human cells and proteins
    plain_language
    An assembly factor prepares copper-binding sites for use.
    primary_references
    [copper-p32061935] COA6 Facilitates Cytochrome c Oxidase Biogenesis as Thiol-reductase for Copper Metallochaperones in Mitochondria. (2020). https://pubmed.ncbi.nlm.nih.gov/32061935/ DOI: 10.1016/j.jmb.2020.01.036
    tissue_or_cell_type
    Mitochondrial intermembrane space

    Copper: transport, cuproenzymes, deficiency, excess and nutrient interactions (2026-09-17) · lines 650–661

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · COA6 knockout HEK293T cells and biochemical protein interaction experiments · source_derived_draft · unverified_draft

    ### copper-coa6-sco1-reduction COA6 acted as a thiol reductase for critical cysteine disulfides in SCO1. Condition category: normal nutrient_topic: Copper research collection; topical membership is not evidence of a direct dietary effect. plain_language: An assembly factor prepares copper-binding sites for use. organism: Human cells and proteins tissue_or_cell_type: Mitochondrial intermembrane space experimental_model: COA6 knockout HEK293T cells and biochemical protein interaction experiments limitations: COA6 machinery failure is not dietary copper depletion. Protein import effects were selective rather than universal loss of all mitochondrial import. exposure: COA6 loss; SCO1/SCO2 disulfide reduction assays evidence_span: {"source_cache": "artifacts/copper-research/32061935.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "7a7828c0b3a9e17878ed230d32af9dd51b667cd1ef0c934fb299f15b5a5e2b0a", "start_char": 0, "end_char": 1043, "text_sha256": "7a7828c0b3a9e17878ed230d32af9dd51b667cd1ef0c934fb299f15b5a5e2b0a"} [copper-p32061935] COA6 Facilitates Cytochrome c Oxidase Biogenesis as Thiol-reductase for Copper Metallochaperones in Mitochondria. (2020). https://pubmed.ncbi.nlm.nih.gov/32061935/ DOI: 10.1016/j.jmb.2020.01.036
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Cu(I)-COX17 with two disulfides transferred copper and two electrons to oxidized SCO1, producing copper-loaded SCO1 and apo-COX17 with three disulfides.

    Human Cu(I)-COX17 with two disulfides → Human SCO1 with oxidized copper-binding cysteines source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/copper-research/18458339.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "1e2740a864c2c21568eae7933027e4c9bb16b985478ebbf946d4d2067ba777f8", "start_char": 0, "end_char": 1482, "text_sha256": "1e2740a864c2c21568eae7933027e4c9bb16b985478ebbf946d4d2067ba777f8"}
    experimental_model
    Purified-protein metal and electron transfer experiments
    exposure
    Defined COX17 and SCO redox states; glutathione reduction
    limitations
    Biochemical transfer mechanism; the same coupled reaction was not observed with SCO2. These results are not proof that glutathione supplementation repairs COX assembly.
    nutrient_topic
    Copper research collection; topical membership is not evidence of a direct dietary effect. · Copper
    organism
    Human proteins
    plain_language
    Copper delivery also changes the receiving protein into a form that can bind it.
    primary_references
    [copper-p18458339] Mitochondrial copper(I) transfer from Cox17 to Sco1 is coupled to electron transfer. (2008). https://pubmed.ncbi.nlm.nih.gov/18458339/ DOI: 10.1073/pnas.0800019105
    tissue_or_cell_type
    Mitochondrial intermembrane-space protein system

    Copper: transport, cuproenzymes, deficiency, excess and nutrient interactions (2026-09-17) · lines 611–622

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified-protein metal and electron transfer experiments · source_derived_draft · unverified_draft

    ### copper-cox17-sco1-handoff Cu(I)-COX17 with two disulfides transferred copper and two electrons to oxidized SCO1, producing copper-loaded SCO1 and apo-COX17 with three disulfides. Condition category: normal nutrient_topic: Copper research collection; topical membership is not evidence of a direct dietary effect. plain_language: Copper delivery also changes the receiving protein into a form that can bind it. organism: Human proteins tissue_or_cell_type: Mitochondrial intermembrane-space protein system experimental_model: Purified-protein metal and electron transfer experiments limitations: Biochemical transfer mechanism; the same coupled reaction was not observed with SCO2. These results are not proof that glutathione supplementation repairs COX assembly. exposure: Defined COX17 and SCO redox states; glutathione reduction evidence_span: {"source_cache": "artifacts/copper-research/18458339.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "1e2740a864c2c21568eae7933027e4c9bb16b985478ebbf946d4d2067ba777f8", "start_char": 0, "end_char": 1482, "text_sha256": "1e2740a864c2c21568eae7933027e4c9bb16b985478ebbf946d4d2067ba777f8"} [copper-p18458339] Mitochondrial copper(I) transfer from Cox17 to Sco1 is coupled to electron transfer. (2008). https://pubmed.ncbi.nlm.nih.gov/18458339/ DOI: 10.1073/pnas.0800019105
    Complete structured claim and evidence

  2. SCO2 overexpression suppressed the cellular copper-deficiency phenotype; SCO1 overexpression did not provide the same rescue.

    Human cytochrome c oxidase assembly protein SCO2 → Biochemically low copper status source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_span
    {"source_cache": "artifacts/copper-research/17189203.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "7653227df0fe557c484a72eafed6a7a96dc06f5d4f63f7eea4a5b9568949a698", "start_char": 0, "end_char": 950, "text_sha256": "7653227df0fe557c484a72eafed6a7a96dc06f5d4f63f7eea4a5b9568949a698"}
    experimental_model
    SCO1/SCO2 patient-cell analysis and genetic complementation
    exposure
    Pathogenic SCO variants; transporter and rescue assays
    limitations
    Copper effects varied with allele and tissue. A genetic assembly defect does not prove inadequate intake or universal response to copper supplementation.
    nutrient_topic
    Copper research collection; topical membership is not evidence of a direct dietary effect. · Copper
    organism
    Human
    plain_language
    Similar-looking proteins are not interchangeable repairs.
    primary_references
    [copper-p17189203] The human cytochrome c oxidase assembly factors SCO1 and SCO2 have regulatory roles in the maintenance of cellular copper homeostasis. (2007). https://pubmed.ncbi.nlm.nih.gov/17189203/ DOI: 10.1016/j.cmet.2006.12.001
    tissue_or_cell_type
    Patient-derived cellular systems
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Copper: transport, cuproenzymes, deficiency, excess and nutrient interactions (2026-09-17) · lines 728–739

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · SCO1/SCO2 patient-cell analysis and genetic complementation · source_derived_draft · unverified_draft

    ### copper-sco2-rescue-specificity SCO2 overexpression suppressed the cellular copper-deficiency phenotype; SCO1 overexpression did not provide the same rescue. Condition category: machinery_impairment nutrient_topic: Copper research collection; topical membership is not evidence of a direct dietary effect. plain_language: Similar-looking proteins are not interchangeable repairs. organism: Human tissue_or_cell_type: Patient-derived cellular systems experimental_model: SCO1/SCO2 patient-cell analysis and genetic complementation limitations: Copper effects varied with allele and tissue. A genetic assembly defect does not prove inadequate intake or universal response to copper supplementation. exposure: Pathogenic SCO variants; transporter and rescue assays evidence_span: {"source_cache": "artifacts/copper-research/17189203.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "7653227df0fe557c484a72eafed6a7a96dc06f5d4f63f7eea4a5b9568949a698", "start_char": 0, "end_char": 950, "text_sha256": "7653227df0fe557c484a72eafed6a7a96dc06f5d4f63f7eea4a5b9568949a698"} [copper-p17189203] The human cytochrome c oxidase assembly factors SCO1 and SCO2 have regulatory roles in the maintenance of cellular copper homeostasis. (2007). https://pubmed.ncbi.nlm.nih.gov/17189203/ DOI: 10.1016/j.cmet.2006.12.001
    Complete structured claim and evidence

In the sources

Preserved passages that mention this component, quoted exactly. Open one to read it in context.

    This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.

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